SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_066328676.1 NCBI__GCF_900100165.1:WP_066328676.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

O81852 Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic; AK-HD 2; AK-HSDH 2; Beta-aspartyl phosphate homoserine 2; EC 2.7.2.4; EC 1.1.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 100% coverage: 1:800/803 of query aligns to 89:909/916 of O81852

query
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O81852

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A

I441 (= I335) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
Q443 (= Q337) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
I522 (≠ F412) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
Q524 (≠ N414) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.

2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
37% identity, 49% coverage: 3:392/803 of query aligns to 3:408/464 of 2hmfA

query
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2hmfA

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binding adenosine-5'-diphosphate: G7 (= G7), T229 (= T215), D230 (≠ H216), V231 (= V217), Y235 (= Y221), T237 (≠ A223), D238 (≠ N224), P239 (= P225), R240 (≠ D226), K265 (≠ T251), V266 (≠ I252)
binding aspartic acid: S39 (= S39), T45 (= T45), F192 (= F178), R206 (= R192), G207 (≠ N193), S209 (= S195)

3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
37% identity, 49% coverage: 3:392/803 of query aligns to 3:403/458 of 3c1nA

query
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3c1nA

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N

R

K

H

V

V

V

A

S

K

I

I

I

V

T

T

D

K

K

R

V

K

N

K

Q

E

G

D

E

D

K

D

I

V

A

V

I

V

V

V

S

S

A

A

R

M

G

S

N

E

A

V

T

T

D

N

E

A

L

L

E

V

E

E

I

I

L

S

A

Q

V

Q

A

A

S

L

K

D

N

V

A

R

D

D

Y

I

K

A

S

K

L

V

L

G

E

D

Q

F

F

I

K

K

K

F

Y

I

Q

R

Q

E

D

K

V

H

Y

Y

A

K

N

A

V

I

D

E

-

E

-

A

L

I

S

S

E

E

F

I

A

K

V

E

-

E

-

V

-

K

-

I

-

D

-

S

-

R

-

I

-

E

L

L

D

E

K

K

L

V

F

L

E

I

G

G

V

V

S

A

L

Y

I

L

G

G

D

E

Y

L

S

T

S

P

K

K

I

S

K

R

D

D

Q

Y

I

I

L

L

S

S

I

F

G

G

E

E

L

R

L

L

S

S

A

S

K

P

L

I

L

L

T

S

A

G

I

A

L

I

V

R

E

D

K

L

G

G

V

E

N

K

A

S

-

I

R

A

F

L

A

E

D

G

S

G

R

E

T

A

F

G

L

I

K

I

T

T

D

D

S

N

K

N

F

F

G

G

D

S

A

A

Q

R

P

V

L

K

E

R

Q

L

V

E

S

V

K

K

K

E

N

R

V

L

I

L

K

P

Y

L

F

L

K

K

D

E

N

G

D

-

A

I

V

I

N

P

V

V

T

T

G

G

F

F

I

I

G

G

S

T

N

T

I

E

N

E

N

G

V

Y

T

I

T

T

L

L

G

G

R

R

N

G

G

G

S

S

N

D

Y

Y

T

S

A

A

S

A

L

L

L

I

A

G

N

Y

Y

G

L

L

D

D

A

A

K

D

E

I

L

I

Q

E

N

I

Y
x
W

T
|
T

H
x
D

V

V

D

S

G

G

I

V

Y

Y

T

T

A

T

N

D

P

P

D

R

L

L

V

V

A

P

D

T

A

A

K

R

I

I

D

P

H

K

L

L

T

S

F

Y

N

I

E

E

A

A

N

M

E

E

L

L

A

A

N

Y

F

F

G

G

A

A

T

K

I

V

L

L

H

H

A

P

K

R

T

T

I

I

I

E

P

P

L

A

L

M

E

E

K

K

N

G

I

I

P

P

L

I

R

L

I

V

L

K

N

N

T

T

F

F

N

E

H

P

E

E

N

S

E

E

G

G

T

T

L

L

I

I

T

T

A

N

T

D

S

M

K

D

S

S

G

-

G

I

I

V

K

K

T

A

L

I

S

S

V

T

L

I

E

K

D

N

L

V

A

A

L

L

V

I

N

N

L

I

E

F

G

G

R

A

G

G

L

M

L

V

G

G

K

V

T

S

G

G

V

T

D

A

A

A

R

R

I

I

F

F

K

K

V

A

M

L

G

G

D

E

N

E

I

V

S

N

V

V

S

I

I

L

I

I

S

S

Q

Q

G

G

S

S

E

E

R

T

G

N

I

I

G

S

L

L

V

V

A

S

E

E

S

E

Q

D

A

V

T

D

K

K

A

A

M

L

I

K

E

A

L

L

E

K

K

R

E

E

F

F

E

-

N

G

D

D

F

L

Y

N

S

N

K

N

D

L

V

I

N

R

K

D

I

V

S

S

V

V

T

D

D

K

D

D

V

V

S

C

V

V

I

I

S

S

I

V

G

G

Q

A

D

G

L

M

binding threonine: G7 (= G7), G8 (= G8), T9 (≠ K9), S10 (= S10), W227 (≠ Y214), T228 (= T215), D229 (≠ H216)

Sites not aligning to the query:

binding threonine: 406, 409, 410, 423, 424, 429, 433

3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
36% identity, 49% coverage: 3:392/803 of query aligns to 3:412/468 of 3c1mC

query
sites
3c1mC

I

V

L

M

K
|
K

F

F

G
|
G

K

T

S

S

L

V

S

G

N

S

G

G

E

E

G

R

I

I

N

R

K

H

V

V

V

A

S

K

I

I

I

V

T

T

D

K

K

R

V

K

N

K

Q

E

G

D

E

D

K

D

I

V

A

V

I

V

V

V

S
|
S

A

A

R

M

G

S

N

E

A

V

T
|
T

D

N

E

A

L

L

E

V

E

E

I

I

L

S

A

Q

V

Q

A

A

-

L

-

D

-

V

-

R

-

D

-

I

S

A

K

K

N

V

A

G

D

D

Y

F

-

I

K

K

S

F

L

I

L

R

E

E

Q

K

F

H

K

Y

K

K

Y

A

Q

I

Q

E

D

E

V

A

Y

I

A

K

N

S

V

E

D

E

L

I

S

K

E

E

-

V

-

K

-

I

-

D

-

S

-

R

F

I

A

E

V

E

L

L

D

E

K

K

L

V

F

L

E

I

G

G

V

V

S

A

L

Y

I

L

G

G

D

E

Y

L

S

T

S

P

K

K

I

S

K

R

D

D

Q

Y

I

I

L

L

S

S

I

F

G

G

E
|
E

L

R

L

L

S

S

A

S

K

P

L

I

L

L

T

S

A

G

I

A

L

I

V

R

E

D

K

L

G

G

V

E

N

K

A

S

-

I

R

A

F

L

A

E

D

G

S

G

R

E

T

A

F

G

L

I

K

I

T

T

D

D

S

N

K

N

F

F

G

G

D

S

A

A

Q

R

P

V

L

K

E

R

Q

L

V

E

S

V

K

K

K

E

N

R

V

L

I

L

K

P

Y

L

F

L

K

K

D

E

N

G

D

-

A

I

V

I

N

P

V

V

T

T

G

G

F
|
F

I

I

G

G

S

T

N

T

I

E

N

E

N

G

V

Y

T

I

T

T

L

L

G

G

R
|
R

N
x
G

G

G

S
|
S

N

D

Y

Y

T

S

A

A

S

A

L

L

L

I

A

G

N

Y

Y

G

L

L

D

D

A

A

K

D

E

I

L

I

Q

E

N

I

Y

W

T
|
T

H
x
D

V

V

D

S

G

G

I

V

Y
|
Y

T

T

A

T

N
x
D

P
|
P

D
x
R

L

L

V

V

A

P

D

T

A

A

K

R

I

I

D

P

H

K

L

L

T

S

F

Y

N

I

E

E

A

A

N

M

E

E

L

L

A

A

N

Y

F

F

G

G

A

A

T
x
K

I
x
V

L

L

H

H

A

P

K

R

T

T

I

I

I

E

P

P

L

A

L

M

E

E

K

K

N

G

I

I

P

P

L

I

R

L

I

V

L

K

N

N

T

T

F

F

N

E

H

P

E

E

N

S

E

E

G

G

T

T

L

L

I

I

T

T

A

N

T

D

S

M

K

E

S

M

G

S

G

D

-

S

-

I

I

V

K

K

T

A

L

I

S

S

V

T

L

I

E

K

D

N

L

V

A

A

L

L

V

I

N

N

L

I

E

F

G

G

R

A

G

G

L

M

L

V

G

G

K

V

T

S

G

G

V

T

D

A

A

A

R

R

I

I

F

F

K

K

V

A

M

L

G

G

D

E

N

E

I

V

S

N

V

V

S

I

I

L

I

I

S

S

Q

Q

G

G

S

S

E

E

R

T

G

N

I

I

G

S

L

L

V

V

A

S

E

E

S

E

Q

D

A

V

T

D

K

K

A

A

M

L

I

K

E

A

L

L

E

K

K

R

E

E

F

F

-

G

-

D

-

G

E

K

N

K

D

S

F

F

Y

L

S

N

K

N

D

N

-

L

V

I

N

R

K

D

I

V

S

S

V

V

T

D

D

K

D

D

V

V

S

C

V

V

I

I

S

S

I

V

G

G

Q

A

D

G

L

M

binding phosphoaminophosphonic acid-adenylate ester: K5 (= K5), G7 (= G7), G8 (= G8), S39 (= S39), T229 (= T215), D230 (≠ H216), Y235 (= Y221), D238 (≠ N224), P239 (= P225), R240 (≠ D226), K265 (≠ T251), V266 (≠ I252)
binding aspartic acid: T45 (= T45), E129 (= E114), F192 (= F178), R206 (= R192), G207 (≠ N193), S209 (= S195)

O94671 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
37% identity, 44% coverage: 448:799/803 of query aligns to 8:364/376 of O94671

query
sites
O94671

I

V

N

N

I

V

A

A

V

I

F

V

G

G

H

T

G

G

L

N

V

I

G

G

T

E

L

L

I

L

N

N

Q

Q

I

I

L

K

E

G

S

F

A

N

K

E

A

N

I

A

E

S

K

T

R

N

K

G

D

T

I

T

K

S

L

F

N

N

I

V

F

V

A

A

I

I

A

S

N

S

S

M

K

E

N

G

V

H

L

Y

L

V

N

S

K

K

D

D

G

Y

V

Q

S

P

P

I

N

N

-

L

-

S

-

E

W

W

V

K

N

N

E

L

I

T

Q

S

T

Q

N

N

G

Q

F

G

A

A

Y

Y

T

S

I

L

K

D

D

A

V

L

I

V

A

D

Y

F

A

L

N

A

E

K

N

S

H

P

L

L

E

P

N

A

L

I

I

L

A

-

V

V

D

D

N

N

T

T

A

A

S

S

A

E

A

A

F

I

V

A

E

Q

N

S

Y

Y

I

P

P

K

L

F

V

L

E

S

N

K

G

K

F

I

D

N

L

I

I

A

S

T

S

P

N

N

K

K

V

K

A

A

N

F

T

S

L

A

S

S

Y

N

G

D

F

V

Y

Y

K

Q

E

N

L

I

R

I

K

K

V

A

L

S

A

K

E

E

N

S

Q

G

K

A

N

L

Y

L

L

M

Y

H

E

E

T

A

N

S

V

V

G

G

A

A

G

G

L

L

P

P

L

I

I

I

D

S

T

T

I

L

K

K

L

E

L

L

H

I

L

A

S

T

G

G

E

D

N

E

I

I

T

I

K

K

I

I

K

E

G

G

V

I

F

F

S

S

G

G

T

T

L

L

S

S

Y

Y

L

I

F

F

N

N

N

V

F

W

S

S

A

P

K

N

-

G

-

K

-

G

D

T

A

A

P
x
S

F

F

S

S

D

D

I

I

L

V

K

K

E

I

A

A

I

K

D

Q

N

N

G

G

Y

Y

T

T

E

E

P

P

D

D

P

P

R

R

E

D

D

D

L

L

C

N

G

G

N

M

D

D

V

V

G

A

R

R

K

K

L

V

L

T

I

I

L

L

A

S

R

R

E

I

L

A

D

G

L

V

Q

H

N

V

E

E

-

S

F

A

E

S

I

F

A

P

I

V

Q

K

N

S

L

L

I

I

P

P

E

E

H

P

L

L

R

K

E

S

G

A

-

V

S

N

A

A

A

E

D

E

F

F

L

L

T

A

K

G

L

L

K

P

E

N

F

F

D

D

P

S

I

E

Y

F

T

A

K

S

I

M

K

R

E

E

-

A

Q

E

K

K

P

E

N

G

H

K

V

V

L

V

R

R

Y

F

I

V

G

G

E

E

L

-

S

-

G

A

D

D

L

V

Q

A

N

N

D

K

K

T

G

T

I

L

L

-

E

-

V

V

K

K

L

L

V

E

S

K

V

Y

P

D

S

A

D

S

T

H

A

P

L

F

G

A

G

N

L

L

K

Q

G

S

S

S

D

D

S

N

F

I

E

S

I

F

Y

T

T

T

E

K

S

R

Y

Y

G

H

D

T

R

R

P

P

I

L

V

V

I

V

Q

I

G

G

A

A

G

G

A

A

G

G

S

A

A

A

V

V

T

T

A

A

R

A

G

G

V

V

F

L

G

G

D

D

I

M

L

I

R

K

L

I

S201 (≠ P635) modified: Phosphoserine

1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
37% identity, 45% coverage: 445:802/803 of query aligns to 2:357/358 of 1tveA

query
sites
1tveA

S

T

K

K

K

V

I

V

N

N

I

V

A

A

V

V

F

I

G

G

H

A

G

G

L

V

V

V

G

G

G

S

T

A

L

F

I

L

N

D

Q

Q

I

L

L

L

E

A

S

-

A

-

K

-

A

-

I

-

E

-

K

M

R

K

K

S

D

T

I

I

K

T

L

Y

N

N

I

L

F

V

A

L

I

L

A

A

N

E

S

A

K

E

N

R

V

S

L

L

L

I

N

S

K

K

D

D

-

F

-

S

-

P

-

L

G

N

V

V

S

G

P

S

N

D

W

W

V

K

N

A

E

A

I

L

Q

A

T

A

N

S

G

T

F

T

-

K

A

T

Y

L

T

P

I

L

K

D

D

D

V

L

I

I

A

A

Y

H

A

L

N

K

E

T

N

S

H

P

L

-

E

K

N

P

L

V

I

I

A

L

V

V

D

D

N

N

T

T

A
x
S

S

S

A

A

A

Y

F

I

V

A

E

G

N

F

Y

Y

I

T

P

K

L

F

V

V

E

E

N

N

G

G

F

I

D

S

L

I

I

A

S

T

S

P

N

N

K
|
K

V

K

A

A

N

F

T

S

L

S

S

D

Y

L

G

A

F

T

Y

W

K

K

E

A

L

L

R

F

K

S

V

N

L

K

A

P

E

T

N

N

Q

G

K

F

N

V

Y

Y

L

-

Y

H

E

E

T

A

N

T

V

V

G

G

A

A

G

G

L

L

P

P

L

I

I

I

D

S

T

F

I

L

K

R

L

E

L

I

H

I

L

Q

S

T

G

G

E

D

N

E

I

V

T

E

K

K

I

I

K

E

G

G

V

I

F

F

S

S

G

G

T
|
T

L

L

S

S

Y

Y

L

I

F

F

N

N

N

E

F

F

S

S

-

T

-

S

-

Q

A

A

K

N

D

D

A

V

P

K

F

F

S

S

D

D

I

V

L

V

K

K

E

V

A

A

I

K

D

K

N

L

G

G

Y

Y

T

T

E

E

P

P

D

D

P

P

R

R

E

D

D
|
D

L

L

C

N

G

G

N

L

D
|
D

V

V

G

A

R

R

K
|
K

L

V

L

T

I

I

L

V

A

G

R

R

-

I

-

S

-

G

-

V

E

E

L

V

D

E

L

S

Q

P

N

T

E

S

F

F

E

-

I

-

A

P

I

V

Q

Q

N

S

L

L

I

I

P

P

E

K

H

P

L

L

R

E

E

S

G

V

S

K

A

S

A

A

D

D

-

E

F

F

L

L

T

E

K

K

L

L

K

S

E

D

F

Y

D

D

P

K

I

D

Y

L

T

T

K

Q

I

L

K

K

E

K

E

E

Q

A

K

A

P

T

-

E

N

N

H

K

V

V

L

L

R

R

Y

F

I

I

G

G

E

K

L

V

S

D

G

V

D

A

L

T

Q

K

N

S

D

V

K

S

G

V

I

G

L

I

E

E

V

K

K

Y

L

D

V

Y

S

S

V

H

P

P

S

-

D

-

T

-

A

-

L

F

G

A

G

S

L

L

K

K

G

G

S

S

D

D

S

N

F

V

F

I

E

S

I

I

Y

K

T

T

E

K

S

R

Y

Y

G

T

D

N

R

-

P

P

I

V

V

V

I

I

Q

Q

G

G

A

A

G

G

A

A

G

G

S

A

A

A

V

V

T

T

A

A

R

A

G

G

V

V

F

L

G

G

D

D

I

V

L

I

R

K

L

I

S

A

D

Q

K

R

active site: D218 (= D661), K222 (= K665)
binding 4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol: S93 (≠ A538), K116 (= K561), T175 (= T621), D213 (= D656), D218 (= D661)

1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
37% identity, 45% coverage: 445:802/803 of query aligns to 2:357/358 of 1q7gA

query
sites
1q7gA

S

T

K

K

K

V

I

V

N

N

I

V

A

A

V

V

F

I

G

G

H

A

G
|
G

L
x
V

V
|
V

G

G

G

S

T

A

L

F

I

L

N

D

Q

Q

I

L

L

L

E

A

S

-

A

-

K

-

A

-

I

-

E

-

K

M

R

K

K

S

D

T

I

I

K

T

L

Y

N

N

I

L

F

V

A

L

I

L

A

A

N
x
E

S

A

K

E

N

R

V

S

L

L

L

I

N

S

K

K

D

D

-

F

-

S

-

P

-

L

G

N

V

V

S

G

P

S

N

D

W

W

V

K

N

A

E

A

I

L

Q

A

T

A

N

S

G

T

F

T

-

K

A

T

Y

L

T

P

I

L

K

D

D

D

V

L

I

I

A

A

Y

H

A

L

N

K

E

T

N

S

H

P

L

-

E

K

N

P

L

V

I

I

A

L

V

V

D

D

N
|
N

T
|
T

A
x
S

S

S

A

A

A

Y

F
x
I

V

A

E

G

N

F

Y

Y

I

T

P

K

L

F

V

V

E

E

N

N

G

G

F

I

D

S

L

I

I

A

S

T

S
x
P

N

N

K
|
K

V

K

A

A

N

F

T

S

L

S

S

D

Y

L

G

A

F

T

Y

W

K

K

E

A

L

L

R

F

K

S

V

N

L

K

A

P

E

T

N

N

Q

G

K

F

N

V

Y

Y

L

-

Y

H

E

E

T
x
A

N

T

V

V

G

G

A

A

G

G

L

L

P

P

L

I

I

I

D

S

T

F

I

L

K

R

L

E

L

I

H

I

L

Q

S

T

G

G

E

D

N

E

I

V

T

E

K

K

I

I

K

E

G

G

V

I

F

F

S
|
S

G

G

T

T

L

L

S

S

Y

Y

L

I

F

F

N

N

N

E

F

F

S

S

-

T

-

S

-

Q

A

A

K

N

D

D

A

V

P

K

F

F

S

S

D

D

I

V

L

V

K

K

E

V

A

A

I

K

D

K

N

L

G

G

Y

Y

T

T

E

E

P

P

D

D

P

P

R

R

E

D

D

D

L

L

C

N

G

G

N

L

D
|
D

V

V

G

A

R

R

K
|
K

L

V

L

T

I

I

L

V

A

G

R

R

-

I

-

S

-

G

-

V

E

E

L

V

D

E

L

S

Q

P

N

T

E

S

F

F

E

-

I

-

A

P

I

V

Q

Q

N

S

L

L

I

I

P

P

E

K

H

P

L

L

R

E

E

S

G

V

S

K

A

S

A

A

D

D

-

E

F

F

L

L

T

E

K

K

L

L

K

S

E

D

F

Y

D

D

P

K

I

D

Y

L

T

T

K

Q

I

L

K

K

E

K

E

E

Q

A

K

A

P

T

-

E

N

N

H

K

V

V

L

L

R

R

Y

F

I

I

G

G

E

K

L

V

S

D

G

V

D

A

L

T

Q

K

N

S

D

V

K

S

G

V

I

G

L

I

E

E

V

K

K

Y

L

D

V

Y

S

S

V

H

P

P

S

-

D

-

T

-

A

-

L

F

G

A

G

S

L

L

K

K

G

G

S

S

D

D

S

N

F

V

F

I

E

S

I

I

Y

K

T

T

E

K

S

R

Y

Y

G

T

D

N

R

-

P

P

I

V

V

V

I

I

Q

Q

G

G

A

A

G

G

A
|
A

G

G

S

A

A

A

V

V

T
|
T

A

A

R

A

G

G

V

V

F

L

G

G

D

D

I

V

L

I

R

K

L

I

S

A

D

Q

K

R

active site: D218 (= D661), K222 (= K665)
binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G456), V14 (≠ L457), V15 (= V458), E39 (≠ N488), N91 (= N536), T92 (= T537), S93 (≠ A538), I97 (≠ F542), P114 (≠ S559), K116 (= K561), A143 (≠ T589), S173 (= S619), K222 (= K665), A338 (= A783), T343 (= T788)

1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
37% identity, 45% coverage: 445:802/803 of query aligns to 2:357/358 of 1ebuD

query
sites
1ebuD

S

T

K

K

K

V

I

V

N

N

I

V

A

A

V

V

F

I

G
|
G

H
x
A

G
|
G

L
x
V

V
|
V

G

G

G

S

T

A

L

F

I

L

N

D

Q

Q

I

L

L

L

E

A

S

-

A

-

K

-

A

-

I

-

E

-

K

M

R

K

K

S

D

T

I

I

K

T

L

Y

N

N

I

L

F

V

A

L

I

L

A

A

N
x
E

S
x
A

K

E

N

R

V

S

L

L

L

I

N

S

K

K

D

D

-

F

-

S

-

P

-

L

G

N

V

V

S

G

P

S

N

D

W

W

V

K

N

A

E

A

I

L

Q

A

T

A

N

S

G

T

F

T

-

K

A

T

Y

L

T

P

I

L

K

D

D

D

V

L

I

I

A

A

Y

H

A

L

N

K

E

T

N

S

H

P

L

-

E

K

N

P

L

V

I

I

A

L

V

V

D

D

N
|
N

T

T

A
x
S

S

S

A

A

A

Y

F

I

V

A

E

G

N

F

Y

Y

I

T

P

K

L

F

V

V

E

E

N

N

G

G

F

I

D

S

L

I

I

A

S

T

S

P

N

N

K
|
K

V

K

A

A

N

F

T

S

L

S

S

D

Y

L

G

A

F

T

Y

W

K

K

E

A

L

L

R

F

K

S

V

N

L

K

A

P

E

T

N

N

Q

G

K

F

N

V

Y

Y

L

-

Y

H

E

E

T

A

N

T

V

V

G

G

A

A

G

G

L

L

P

P

L

I

I

I

D

S

T

F

I

L

K

R

L

E

L

I

H

I

L

Q

S

T

G

G

E

D

N

E

I

V

T

E

K

K

I

I

K

E

G

G

V

I

F

F

S

S

G

G

T

T

L

L

S

S

Y

Y

L

I

F

F

N

N

N

E

F

F

S

S

-

T

-

S

-

Q

A

A

K

N

D

D

A

V

P

K

F

F

S

S

D

D

I

V

L

V

K

K

E

V

A

A

I

K

D

K

N

L

G

G

Y

Y

T

T

E

E

P

P

D

D

P

P

R

R

E

D

D

D

L

L

C

N

G

G

N

L

D
|
D

V

V

G

A

R

R

K
|
K

L

V

L

T

I

I

L

V

A

G

R

R

-

I

-

S

-

G

-

V

E

E

L

V

D

E

L

S

Q

P

N

T

E

S

F

F

E

-

I

-

A

P

I

V

Q

Q

N

S

L

L

I

I

P

P

E

K

H

P

L

L

R

E

E

S

G

V

S

K

A

S

A

A

D

D

-

E

F

F

L

L

T

E

K

K

L

L

K

S

E

D

F

Y

D

D

P

K

I

D

Y

L

T

T

K

Q

I

L

K

K

E

K

E

E

Q

A

K

A

P

T

-

E

N

N

H

K

V

V

L

L

R

R

Y

F

I

I

G

G

E

K

L

V

S

D

G

V

D

A

L

T

Q

K

N

S

D

V

K

S

G

V

I

G

L

I

E

E

V

K

K

Y

L

D

V

Y

S

S

V

H

P

P

S

-

D

-

T

-

A

-

L

F

G

A

G

S

L

L

K

K

G

G

S

S

D

D

S

N

F

V

F

I

E

S

I

I

Y

K

T

T

E

K

S

R

Y

Y

G

T

D

N

R

-

P

P

I

V

V

V

I

I

Q

Q

G

G

A

A

G

G

A

A

G

G

S

A

A

A

V

V

T
|
T

A

A

R

A

G

G

V

V

F

L

G

G

D

D

I

V

L

I

R

K

L

I

S

A

D

Q

K

R

active site: D218 (= D661), K222 (= K665)
binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G454), A12 (≠ H455), G13 (= G456), V14 (≠ L457), V15 (= V458), E39 (≠ N488), A40 (≠ S489), N91 (= N536), S93 (≠ A538), K116 (= K561), T343 (= T788)

1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
37% identity, 45% coverage: 445:802/803 of query aligns to 2:357/358 of 1ebfA

query
sites
1ebfA

S

T

K

K

K

V

I

V

N

N

I

V

A

A

V

V

F
x
I

G

G

H
x
A

G
|
G

L
x
V

V
|
V

G

G

G

S

T

A

L

F

I

L

N

D

Q

Q

I

L

L

L

E

A

S

-

A

-

K

-

A

-

I

-

E

-

K

M

R

K

K

S

D

T

I

I

K

T

L

Y

N

N

I

L

F

V

A

L

I

L

A

A

N
x
E

S
x
A

K

E

N

R

V

S

L

L

L

I

N

S

K

K

D

D

-

F

-

S

-

P

-

L

G

N

V

V

S

G

P

S

N

D

W

W

V

K

N

A

E

A

I

L

Q

A

T

A

N

S

G

T

F

T

-

K

A

T

Y

L

T

P

I

L

K

D

D

D

V

L

I

I

A

A

Y

H

A

L

N

K

E

T

N

S

H

P

L

-

E

K

N

P

L

V

I

I

A

L

V

V

D

D

N

N

T
|
T

A
x
S

S

S

A

A

A

Y

F

I

V

A

E

G

N

F

Y

Y

I

T

P

K

L

F

V

V

E

E

N

N

G

G

F

I

D

S

L

I

I

A

S

T

S
x
P

N

N

K

K

V

K

A

A

N

F

T

S

L

S

S

D

Y

L

G

A

F

T

Y

W

K

K

E

A

L

L

R

F

K

S

V

N

L

K

A

P

E

T

N

N

Q

G

K

F

N

V

Y

Y

L

-

Y

H

E

E

T

A

N

T

V

V

G

G

A

A

G

G

L

L

P

P

L

I

I

I

D

S

T

F

I

L

K

R

L

E

L

I

H

I

L

Q

S

T

G

G

E

D

N

E

I

V

T

E

K

K

I

I

K

E

G

G

V

I

F

F

S

S

G

G

T

T

L

L

S

S

Y

Y

L

I

F

F

N

N

N

E

F

F

S

S

-

T

-

S

-

Q

A

A

K

N

D

D

A

V

P

K

F

F

S

S

D

D

I

V

L

V

K

K

E

V

A

A

I

K

D

K

N

L

G

G

Y

Y

T

T

E

E

P

P

D

D

P

P

R

R

E

D

D

D

L

L

C

N

G

G

N

L

D
|
D

V

V

G

A

R

R

K
|
K

L

V

L

T

I

I

L

V

A

G

R

R

-

I

-

S

-

G

-

V

E

E

L

V

D

E

L

S

Q

P

N

T

E

S

F

F

E

-

I

-

A

P

I

V

Q

Q

N

S

L

L

I

I

P

P

E

K

H

P

L

L

R

E

E

S

G

V

S

K

A

S

A

A

D

D

-

E

F

F

L

L

T

E

K

K

L

L

K

S

E

D

F

Y

D

D

P

K

I

D

Y

L

T

T

K

Q

I

L

K

K

E

K

E

E

Q

A

K

A

P

T

-

E

N

N

H

K

V

V

L

L

R

R

Y

F

I

I

G

G

E

K

L

V

S

D

G

V

D

A

L

T

Q

K

N

S

D

V

K

S

G

V

I

G

L

I

E

E

V

K

K

Y

L

D

V

Y

S

S

V

H

P

P

S

-

D

-

T

-

A

-

L

F

G

A

G

S

L

L

K

K

G

G

S

S

D

D

S

N

F

V

F

I

E

S

I

I

Y

K

T

T

E

K

S

R

Y

Y

G

T

D

N

R

-

P

P

I

V

V

V

I

I

Q

Q

G

G

A

A

G

G

A

A

G

G

S

A

A

A

V

V

T

T

A

A

R

A

G

G

V

V

F

L

G

G

D

D

I

V

L

I

R

K

L

I

S

A

D

Q

K

R

active site: D218 (= D661), K222 (= K665)
binding nicotinamide-adenine-dinucleotide: I10 (≠ F453), A12 (≠ H455), G13 (= G456), V14 (≠ L457), V15 (= V458), E39 (≠ N488), A40 (≠ S489), T92 (= T537), S93 (≠ A538), P114 (≠ S559)

P31116 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
37% identity, 45% coverage: 445:802/803 of query aligns to 3:358/359 of P31116

query
sites
P31116

S

T

K

K

K

V

I

V

N

N

I

V

A

A

V

V

F

I

G

G

H
x
A

G

G

L
x
V

V
|
V

G

G

G

S

T

A

L

F

I

L

N

D

Q

Q

I

L

L

L

E

A

S

-

A

-

K

-

A

-

I

-

E

-

K

M

R

K

K

S

D

T

I

I

K

T

L

Y

N

N

I

L

F

V

A

L

I

L

A

A

N

E

S
x
A

K

E

N

R

V

S

L

L

L

I

N

S

K

K

D

D

-

F

-

S

-

P

-

L

G

N

V

V

S

G

P

S

N

D

W

W

V

K

N

A

E

A

I

L

Q

A

T

A

N

S

G

T

F

T

-

K

A

T

Y

L

T

P

I

L

K

D

D

D

V

L

I

I

A

A

Y
x
H

A

L

N

K

E

T

N

S

H

P

L

-

E

K

N

P

L

V

I

I

A

L

V

V

D

D

N

N

T
|
T

A

S

S

S

A

A

A

Y

F

I

V

A

E

G

N

F

Y

Y

I

T

P

K

L

F

V

V

E

E

N

N

G

G

F

I

D

S

L

I

I

A

S

T

S

P

N

N

K
|
K

V

K

A

A

N

F

T

S

L

S

S

D

Y

L

G

A

F

T

Y

W

K

K

E

A

L

L

R

F

K

S

V

N

L

K

A

P

E

T

N

N

Q

G

K

F

N

V

Y

Y

L

-

Y

H

E
|
E

T

A

N

T

V
|
V

G

G

A
|
A

G

G

L
|
L

P

P

L

I

I

I

D

S

T

F

I

L

K

R

L

E

L

I

H

I

L

Q

S

T

G

G

E

D

N

E

I

V

T

E

K

K

I

I

K

E

G

G

V

I

F

F

S

S

G

G

T

T

L

L

S

S

Y

Y

L

I

F

F

N

N

N

E

F

F

S

S

-

T

-

S

-

Q

A

A

K

N

D

D

A

V

P

K

F

F

S

S

D

D

I

V

L

V

K

K

E

V

A

A

I

K

D

K

N

L

G

G

Y

Y

T

T

E
|
E

P

P

D

D

P

P

R

R

E

D

D

D

L

L

C

N

G

G

N

L

D
|
D

V

V

G

A

R

R

K
|
K

L

V

L

T

I

I

L

V

A

G

R

R

-

I

-

S

-

G

-

V

E

E

L

V

D

E

L

S

Q

P

N

T

E

S

F

F

E

-

I

-

A

P

I

V

Q

Q

N

S

L

L

I

I

P

P

E

K

H

P

L

L

R

E

E

S

G

V

S

K

A

S

A

A

D

D

-

E

F

F

L

L

T

E

K

K

L

L

K

S

E

D

F

Y

D

D

P

K

I

D

Y

L

T

T

K

Q

I

L

K

K

E

K

E

E

Q

A

K

A

P

T

-

E

N

N

H

K

V

V

L

L

R

R

Y

F

I

I

G

G

E

K

L

V

S

D

G

V

D

A

L

T

Q

K

N

S

D

V

K

S

G

V

I

G

L

I

E

E

V

K

K

Y

L

D

V

Y

S

S

V
x
H

P

P

S

-

D

-

T

-

A

-

L

F

G

A

G

S

L

L

K

K

G

G

S

S

D

D

S

N

F

V

F

I

E

S

I

I

Y

K

T

T

E

K

S

R

Y

Y

G

T

D

N

R

-

P

P

I

V

V

V

I

I

Q

Q

G

G

A

A

G

G

A

A

G
|
G

S

A

A

A

V

V

T

T

A

A

R

A

G

G

V

V

F

L

G

G

D

D

I

V

L

I

R

K

L

I

S

A

D

Q

K

R

A13 (≠ H455) binding NAD(+)
V15 (≠ L457) binding NAD(+)
V16 (= V458) binding NAD(+)
A41 (≠ S489) binding NAD(+)
H79 (≠ Y522) mutation to A: Reduces kcat 2-fold.
T93 (= T537) binding NAD(+)
K117 (= K561) mutation to A: Loss of activity.
E143 (= E588) binding Na(+)
V146 (= V591) binding Na(+)
A148 (= A593) binding Na(+)
L150 (= L595) binding Na(+)
E208 (= E650) binding L-homoserine; mutation to D: Increases KM for aspartate-semialdehyde 48-fold and reduces kcat by 50%.; mutation E->L,Q: Loss of activity.
D219 (= D661) binding L-homoserine; mutation to L: Reduces kcat 150-fold.
K223 (= K665) mutation to V: Loss of activity.
H309 (≠ V748) mutation to A: Reduces kcat 40-fold. Affects dimer formation.
G340 (= G784) binding NAD(+)

2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
28% identity, 55% coverage: 3:442/803 of query aligns to 6:459/470 of 2cdqA

query
sites
2cdqA

I

V

L

M

K

K

F

F

G

G

K

S

S

S

L

V

S

A

N

S

G

A

E

E

G

R

I

M

N

K

K

E

V

V

V

A

S

D

I

L

I

I

T

L

D

-

K

-

V

T

N

F

Q

P

G

E

E

E

K

S

I

P

A

V

I

I

V

V

V

L

S
|
S

A
|
A

R

M

G

G

N

K

A

T

T
|
T

D

N

E

N

L

L

-

L

-

A

-

G

E

E

E

K

I

A

L

V

A

S

V

C

A

G

S

V

K

S

N

N

A

A

D

S

Y

E

K

I

S

E

L

E

L

L

E

S

Q

I

F

I

K

K

K

E

Y

L

Q

H

Q

I

D

R

V

T

Y

V

A

K

N

E

V

L

D

N

L

I

S

D

E

P

E

S

F

V

A

I

V

L

-

T

-

Y

-

L

-

E

L

L

D

E

K

Q

L

L

F

L

E

K

G

G

V

I

S

A

L

M

I

M

G

K

D

E

Y

L

S

T

S

L

K

R

I

T

K

R

D

D

Q

Y

I

L

L

V

S

S

I

F

G

G

E
|
E

L

C

L

L

S

S

A

T

K

R

L

I

L

F

T

A

A

A

I

Y

L

L

V

N

E

T

K

I

G

G

V

V

N

K

A

A

R

R

F

Q

A

Y

D

D

S

A

R

F

T

E

-

I

-

G

F

F

L

I

K

T

T

T

D

D

S

D

K

-

F

F

G

T

D

N

A

G

Q

D

P

I

L

L

E

E

Q

A

V

T

S

Y

K

P

K

A

N

V

V

A

I

K

K

R

Y

L

F

Y

K

D

D

D

-

W

-

M

N

H

D

D

D

P

A

A

V

V

N

P

V

I

V

V

T

T

G

G

F

F

I

L

G

G

S

K

N

G

I

W

N

K

N

T

-

G

V

A

T

V

T

T

L

L

G

G

R

R

N

G

G

G

S

S

N

D

Y

L

T

T

A

A

S

T

L

T

L

I

A

G

N

K

Y

A

L

L

D

G

A

L

K

K

E

E

L

I

Q

Q

N

V

Y

W

T

K

H

D

V

V

D

D

G

G

I

V

Y

L

T

T

A

C

N

D

P

P

D

T

L

I

V

Y

A

K

D

R

A

A

K

T

K

P

I

V

D

P

H

Y

L

L

T

T

F

F

N

D

E

E

A

A

N

A

E

E

L

L

A

A

N

Y

F

F

G

G

A

A

T

Q

I

V

L

L

H

H

A

P

K

Q

T

S

I

M

I

R

P

P

L

A

L

R

E

E

K

G

N

E

I

I

P

P

L

V

R

R

I

V

L

K

N

N

T

S

F

Y

N

N

H

P

E

K

N

A

E

P

G

G

T

T

L

I

I

I

T

T

A

K

T

T

S

R

-

D

K

M

S

T

G

K

G

S

I

I

K

L

T

T

L

S

S

I

V

V

L

L

E

K

-

R

D

N

L

V

A

T

L

M

V

L

N

D

L

I

E

A

G

S

R

T

G

R

L
x
M

L

L

G

G

K
x
Q

T

V

G

G

V
x
F

D
x
L

A

A

R

K

I

V

F

F

K

S

V

I

M

F

G

E

D

E

N

L

N
x
G

I
|
I

S
|
S

V
|
V

S
x
D

I

V

S

A

Q

-

G

-

S

T

S

S

E

E

R

V

G

S

I

I

G

S

L

L

V

T

V

L

A

D

E

P

S

S

Q

K

-

L

A
x
W

T
x
S

K
x
R

A

E

M
x
L

I

I

E

Q

L

Q

E
|
E

K

L

E

-

F

-

E

-

N

-

D

D

F

H

Y

V

S

V

K

E

D

E

V

L

N

E

K

K

I

I

S

A

V

V

T

V

D

N

D

L

V

L

-

K

-

G

-

R

S

A

V

I

I

I

S

S

I

L

I

I

G

G

Q

N

D

-

L

-

S

-

T

-

F

-

Y

-

R

V

P

Q

Y

H

T

S

A

S

L

L

I

I

K

L

N

E

K

R

I

A

I

F

P

H

I

V

L

L

F

Y

N

T

N

K

T

G

V

V

T

N

G

V

K

Q

-

M

-

I

-

S

-

Q

-

G

-

A

-

S

-

K

-

V

N

N

V

I

S

S

L

F

V

I

V

V

K

N

K

E

S

A

E

E

L

A

N

E

K

G

A

C

L

V

N

Q

V

A

I

L

H

H

G

K

E

S

I

F

F

F

binding lysine: S40 (= S39), A41 (= A40), T46 (= T45), E124 (= E114), M327 (≠ L311), Q330 (≠ K314), F333 (≠ V317), L334 (≠ D318), S347 (= S331), V348 (= V332), D349 (≠ S333)
binding s-adenosylmethionine: G345 (≠ N329), I346 (= I330), S347 (= S331), W368 (≠ A353), S369 (≠ T354), R370 (≠ K355), L372 (≠ M357), E376 (= E361)

2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
29% identity, 48% coverage: 5:393/803 of query aligns to 6:395/447 of 2j0xA

query
sites
2j0xA

K

K

F

F

G

G

K

T

S

S

L

V

S

A

N

D

G

F

E

D

G

A

I

M

N

N

K

R

V

S

V

A

S

D

I

I

I

V

T

L

D

S

K

D

V

A

N

N

Q

V

G

R

E

-

K

-

I

-

A

L

I

V

V

V

V

L

S

S

A

A

R

S

G

A

N

G

A

I

T

T

D

N

E

L

L

L

E

V

E

A

I

L

L

A

A

E

V

G

A

L

S

E

K

P

N

G

A

E

D

R

Y

F

K

E

S

K

L

L

L

D

E

A

-

I

-

R

-

N

-

I

Q

Q

F

F

K

A

K

I

Y

L

Q

E

Q

R

D

L

V

R

Y

Y

A

P

N

N

V

V

D

-

L

I

S

R

E

E

F

-

A

-

V

-

L

I

D

E

K

R

L

L

F

L

E

E

G

N

V

I

S

T

L

V

I

L

G

A

D

E

-

A

-

L

-

A

Y

T

S

S

S

P

K

A

I

L

K

T

D

D

Q

E

I

L

L

V

S

S

I

H

G

G

E

E

L

L

L

M

S

S

A

T

K

L

L

L

L

F

T

V

A

E

I

I

L

L

V

R

E

E

K

R

G

D

V

V

N

Q

A

A

R

Q

F

W

A

F

D

D

S

V

R

R

T

K

F

V

L

M

K

R

T

T

D

N

S

D

K

R

F

F

G

G

D

R

A

A

Q

E

P

P

-

D

L

I

E

A

Q

A

V

L

S

A

K

E

K

L

N

A

V

A

I

L

K

Q

Y

L

F

L

K

P

D

R

N

L

D

N

D

E

A

G

V

L

N

V

V

I

V

T

T

Q

G

G

F
|
F

I

I

G

G

S

S

N

E

I

N

N

K

N

G

V

R

T

T

L

L

G

G

R

R

N
x
G

G
|
G

S
|
S

N
x
D

Y

Y

T

T

A

A

S

A

L

L

A

A

N

E

Y

A

L

L

D

H

A

A

K

S

E

R

L

V

Q

D

N

I

Y

W

T

T

H

D

V

V

D

P

G

G

I

I

Y

Y

T

T

A

T

N

D

P

P

D

R

L

V

V

V

A

S

D

A

A

A

K

K

K

R

I

I

D

D

H

E

L

I

T

A

F

F

N

A

E

E

A

A

N

A

E

E

L

M

A

A

N

T

F

F

G

G

A

A

T

K

I

V

L

L

H

H

A

P

K

A

T

T

I

L

P

P

L

A

L

V

E

R

K

S

N

D

I

I

P

P

L

V

R

F

I

V

L

G

N

S

T

S

F

K

N

D

H

P

E

R

N

A

E

G

G

G

T

T

L

L

I

V

T

C

A

N

T

K

S

T

K

E

S

N

G

P

I

L

-

F

K

R

T

A

L

L

S

A

V

L

L

R

E

R

D

N

L

Q

A

T

L

L

V

L

N

T

L

L

E

H

G

S

R

L

G

N

L
x
M

L

L

G

H

K
x
S

T

R

G

G

V
x
F

D
x
L

A

A

R

E

I

V

F

F

K

G

V

I

M

L

G

A

D

R

N

H

N

N

I

I

S
|
S

V
|
V

S
x
D

I

L

I

I

S

T

Q

-

G

-

S

T

S
|
S

E
|
E

R

V

G

S

I

V

G

A

L

L

V

T

V

L

A

D

E

T

S

T

Q

G

A

S

T

T

K

S

A

T

M

G

I

D

E

T

L

L

E

L

K

T

E

Q

F

S

E

L

N

L

D

M

F

E

Y

L

S

S

K

A

D

-

V

L

N

C

K

R

I

V

S

E

V

V

T

E

D

E

D

G

V

L

S

A

V

L

I

V

S

A

I

L

I

I

G

G

Q

N

D

D

L

L

S

S

binding aspartic acid: F182 (= F178), G197 (≠ N193), G198 (= G194), S199 (= S195), D200 (≠ N196)
binding lysine: M316 (≠ L311), S319 (≠ K314), F322 (≠ V317), L323 (≠ D318), S336 (= S331), V337 (= V332), D338 (≠ S333), S343 (= S340), E344 (= E341)

2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
29% identity, 48% coverage: 5:393/803 of query aligns to 6:395/447 of 2j0wA

query
sites
2j0wA

K

K

F

F

G

G

K

T

S

S

L

V

S

A

N

D

G

F

E

D

G

A

I

M

N

N

K

R

V

S

V

A

S

D

I

I

I

V

T

L

D

S

K

D

V

A

N

N

Q

V

G

R

E

-

K

-

I

-

A

L

I

V

V

V

V

L

S
|
S

A

A

R

S

G

A

N

G

A

I

T
|
T

D

N

E

L

L

L

E

V

E

A

I

L

L

A

A

E

V

G

A

L

S

E

K

P

N

G

A

E

D

R

Y

F

K

E

S

K

L

L

L

D

E

A

-

I

-

R

-

N

-

I

Q

Q

F

F

K

A

K

I

Y

L

Q

E

Q

R

D

L

V

R

Y

Y

A

P

N

N

V

V

D

-

L

I

S

R

E

E

F

-

A

-

V

-

L

I

D

E

K

R

L

L

F

L

E

E

G

N

V

I

S

T

L

V

I

L

G

A

D

E

-

A

-

L

-

A

Y

T

S

S

S

P

K

A

I

L

K

T

D

D

Q

E

I

L

L

V

S

S

I

H

G

G

E
|
E

L

L

L

M

S

S

A

T

K

L

L

L

L

F

T

V

A

E

I

I

L

L

V

R

E

E

K

R

G

D

V

V

N

Q

A

A

R

Q

F

W

A

F

D

D

S

V

R

R

T

K

F

V

L

M

K

R

T

T

D

N

S

D

K

R

F

F

G

G

D

R

A

A

Q

E

P

P

-

D

L

I

E

A

Q

A

V

L

S

A

K

E

K

L

N

A

V

A

I

L

K

Q

Y

L

F

L

K

P

D

R

N

L

D

N

D

E

A

G

V

L

N

V

V

I

V

T

T

Q

G

G

F
|
F

I

I

G

G

S

S

N

E

I

N

N

K

N

G

V

R

T

T

L

L

G

G

R
|
R

N
x
G

G

G

S
|
S

N

D

Y

Y

T

T

A

A

S

A

L

L

A

A

N

E

Y

A

L

L

D

H

A

A

K

S

E

R

L

V

Q

D

N

I

Y

W

T
|
T

H
x
D

V

V

D

P

G

G

I
|
I

Y
|
Y

T

T

A

T

N
x
D

P

P

D
x
R

L

V

V

V

A

S

D

A

A

A

K

K

K

R

I

I

D

D

H

E

L

I

T

A

F

F

N

A

E

E

A

A

N

A

E

E

L

M

A

A

N

T

F

F

G

G

A

A

T
x
K

I
x
V

L

L

H

H

A

P

K

A

T

T

I

L

P

P

L

A

L

V

E

R

K

S

N

D

I

I

P

P

L

V

R

F

I

V

L

G

N

S

T

S

F

K

N

D

H

P

E

R

N

A

E

G

G

G

T

T

L

L

I

V

T

C

A

N

T

K

S

T

K

E

S

N

G

P

I

L

-

F

K

R

T

A

L

L

S

A

V

L

L

R

E

R

D

N

L

Q

A

T

L

L

V

L

N

T

L

L

E

H

G

S

R

L

G

N

L

M

L

L

G

H

K

S

T

R

G

G

V

F

D

L

A

A

R

E

I

V

F

F

K

G

V

I

M

L

G

A

D

R

N

H

N

N

I

I

S

S

V

V

S

D

I

L

I

I

S

T

Q

-

G

-

S

T

S

S

E

E

R

V

G

S

I

V

G

A

L

L

V

T

V

L

A

D

E

T

S

T

Q

G

A

S

T

T

K

S

A

T

M

G

I

D

E

T

L

L

E

L

K

T

E

Q

F

S

E

L

N

L

D

M

F

E

Y

L

S

S

K

A

D

-

V

L

N

C

K

R

I

V

S

E

V

V

T

E

D

E

D

G

V

L

S

A

V

L

I

V

S

A

I

L

I

I

G

G

Q

N

D

D

L

L

S

S

binding adenosine-5'-diphosphate: T219 (= T215), D220 (≠ H216), I224 (= I220), Y225 (= Y221), D228 (≠ N224), R230 (≠ D226), K255 (≠ T251), V256 (≠ I252)
binding aspartic acid: S37 (= S39), T43 (= T45), E117 (= E114), F182 (= F178), R196 (= R192), G197 (≠ N193), S199 (= S195)

P08660 Lysine-sensitive aspartokinase 3; Aspartate kinase III; AKIII; Lysine-sensitive aspartokinase III; EC 2.7.2.4 from Escherichia coli (strain K12) (see paper)
29% identity, 48% coverage: 5:393/803 of query aligns to 8:397/449 of P08660

query
sites
P08660

K
|
K

F

F

G

G

K

T

S

S

L

V

S

A

N

D

G

F

E

D

G

A

I

M

N

N

K

R

V

S

V

A

S

D

I

I

I

V

T

L

D

S

K

D

V

A

N

N

Q

V

G

R

E

-

K

-

I

-

A

L

I

V

V

V

V

L

S

S

A

A

R

S

G

A

N

G

A

I

T

T

D

N

E

L

L

L

E

V

E

A

I

L

L

A

A

E

V

G

A

L

S

E

K

P

N

G

A

E

D

R

Y

F

K

E

S

K

L

L

L

D

E

A

-

I

-

R

-

N

-

I

Q

Q

F

F

K

A

K

I

Y

L

Q

E

Q

R

D

L

V

R

Y

Y

A

P

N

N

V

V

D

-

L

I

S

R

E

E

F

-

A

-

V

-

L

I

D

E

K

R

L

L

F

L

E

E

G

N

V

I

S

T

L

V

I

L

G

A

D

E

-

A

-

L

-

A

Y

T

S

S

S

P

K

A

I

L

K

T

D

D

Q

E

I

L

L

V

S

S

I

H

G

G

E
|
E

L

L

L

M

S

S

A

T

K

L

L

L

L

F

T

V

A

E

I

I

L

L

V

R

E

E

K

R

G

D

V

V

N

Q

A

A

R

Q

F

W

A

F

D

D

S

V

R

R

T

K

F

V

L

M

K

R

T

T

D

N

S

D

K

R

F

F

G

G

D

R

A

A

Q

E

P

P

-

D

L

I

E

A

Q

A

V

L

S

A

K

E

K

L

N

A

V

A

I

L

K

Q

Y

L

F

L

K

P

D

R

N

L

D

N

D

E

A

G

V

L

N

V

V

I

V

T

T

Q

G

G

F

F

I

I

G

G

S

S

N

E

I

N

N

K

N

G

V

R

T

T

L

L

G

G

R
|
R

N

G

G

G

S

S

N
x
D

Y

Y

T

T

A

A

S

A

L

L

A

A

N

E

Y

A

L

L

D

H

A

A

K

S

E

R

L

V

Q

D

N

I

Y

W

T

T

H

D

V

V

D

P

G

G

I

I

Y

Y

T

T

A

T

N

D

P

P

D

R

L

V

V

V

A

S

D

A

A

A

K

K

K

R

I

I

D

D

H

E

L

I

T

A

F

F

N

A

E

E

A

A

N

A

E

E

L

M

A

A

N

T

F

F

G

G

A

A

T

K

I

V

L

L

H

H

A

P

K

A

T

T

I

L

P

P

L

A

L

V

E

R

K

S

N

D

I

I

P

P

L

V

R

F

I

V

L

G

N

S

T

S

F

K

N

D

H

P

E

R

N

A

E

G

G

G

T

T

L

L

I

V

T

C

A

N

T

K

S

T

K

E

S

N

G

P

I

L

-

F

K

R

T

A

L

L

S

A

V

L

L

R

E

R

D

N

L

Q

A

T

L

L

V

L

N

T

L

L

E

H

G

S

R

L

G

N

L

M

L

L

G

H

K

S

T

R

G

G

V

F

D

L

A

A

R

E

I

V

F

F

K

G

V

I

M

L

G

A

D

R

N

H

N

N

I

I

S

S

V

V

S

D

I

L

I

I

S

T

Q

-

G

-

S

T

S

S

E

E

R

V

G

S

I

V

G

A

L

L

V

T

V

L

A

D

E

T

S

T

Q

G

A

S

T

T

K

S

A

T

M

G

I

D

E

T

L

L

E

L

K

T

E

Q

F

S

E

L

N

L

D

M

F

E

Y

L

S

S

K

A

D

-

V

L

N

C

K

R

I

V

S

E

V

V

T

E

D

E

D

G

V

L

S

A

V

L

I

V

S

A

I

L

I

I

G

G

Q

N

D

D

L

L

S

S

K8 (= K5) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
E119 (= E114) mutation to D: Increases KM for aspartate about 3000-fold.
R198 (= R192) mutation to K: Increases KM for aspartate about 200-fold.
D202 (≠ N196) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.

P10869 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
24% identity, 57% coverage: 3:457/803 of query aligns to 16:515/527 of P10869

query
sites
P10869

I

V

L

Q

K
|
K

F

F

G

G

K

T

S

S

L

V

S
x
G

N
x
K

G

F

E

P

G

-

I

-

N

-

K

-

V

-

V

V

S

Q

I

I

I

V

T

D

D

D

K

I

V

V

N

K

Q

H

G

Y

E

S

K

K

-

P

-

D

-

G

-

P

-

N

I

V

A

A

I

V

V

V

V

C

S

S

A

A

R

R

G

S

N

S

-

Y

-

T

-

K

-

A

-

E

-

G

A

T

T

T

D

S

E

R

L

L

E

L

E

K

I

C

L

C

A

D

V

L

A

A

S

S

K

Q

N

E

A

S

D

E

Y

F

K

Q

S

D

L

I

E

E

Q

V

F

I

K

R

K

Q

Y

D

Q

H

Q

I

D

D

-

N

-

A

-

D

-

R

-

F

-

I

-

L

-

N

-

P

-

A

V

L

Y

Q

A

A

N

K

V

L

-

V

-

D

D

D

L

T

S

N

E

K

E

E

F

L

A

E

V

L

L

V

D

K

K

K

L

Y

F

L

E

N

G

A

V

S

S

K

L

V

I

L

G

G

D

E

Y

V

S

S

K

R

I

T

K

V

D

D

Q

L

I

V

L

M

S

S

I

C

G

G

E

E

L

K

L

L

S

S

A

C

K

L

L

F

L

M

T

T

A

A

I

L

L

C

V

N

E

D

K

R

G

G

V

C

N

K

A

A

R

K

F

Y

A

V

D

D

S

L

R

S

T

H

F

I

L

V

K

P

T

S

D

D

-

F

-

S

-

A

S

S

K

A

F

L

G

D

D

N

A

S

-

F

-

Y

Q

T

P

F

L

L

E

V

Q

Q

V

A

S

L

K

K

K

E

N

K

V

L

I

A

K

P

Y

F

F

V

K

S

D

A

N

K

D

E

D

R

A

I

V

V

N

P

V

V

V

F

T

T

G

G

F

F

I

F

G

G

S

L

N

V

I

P

N

T

N

G

V

L

T

L

T

N

T

G

L

V

G

G

R

R

N

G

G

Y

S

T

N

D

Y

L

T

C

A

A

S

A

L

L

L

I

A

A

N

V

Y

A

L

V

D

N

A

A

K

D

E

E

L

L

Q

Q

N

V

Y

W

T

K

H
x
E

V

V

D

D

G

G

I

I

Y

F

T

T

A

A

N

D

P

P

D

R

L

K

V

V

A

P

D

E

A

A

K

R

K

L

I

L

D

D

H

S

L

V

T

T

F

P

N

E

E
|
E

A

A

N

S

E

E

L

L

A

T

N

Y

F

Y

G

G

A

S

T

E

I

V

L

I

H
|
H

A

P

K

F

T

T

I

M

I

E

P

Q

L

V

L

I

E

R

K

A

N

K

I

I

P

P

L

I

R

R

I

I

L

K

N

N

T

V

F

Q

N

N

H

P

E

L

N

G

E

N

G

G

T

T

L

I

I

I

T

Y

A

P

-

D

-

N

T

V

S

A

K

K

S

K

G

G

-

E

-

S

-

T

-

P

-

H

-

P

-

E

-

N

-

L

-

S

-

F

-

Y

-

E

-

K

-

R

-

K

-

R

G

G

I

A

K

T

T

A

L

I

S

T

V

T

L

K

E

N

D

D

L

I

A

F

L

V

V

I

N

N

L

I

E

H

G

S

R

N

G

K

L

K

L

T

G

L

K

S

T

H

G

G

V

F

D

L

A

A

R

Q

I

I

F

F

K

T

V

I

M

L

G

D

D

K

N

Y

N

K

I

L

S

V

V

V

S

D

I

L

I

I

S

S

Q

T

G

S

S

E

S

V

E

H

R

V

G

S

I

M

G
x
A

L

L

V

P

V

I

A

P

E

D

S

A

Q

D

A

S

T

L

K

K

A

S

M

L

I
x
R

E

Q

L

A

E

E

K

E

E

K

F

L

E

-

N

-

D

-

F

-

Y

-

S

-

K

R

D

I

V

L

N

G

K

S

I

V

S

D

V

I

T

T

D

K

V

L

S

S

V

I

I

V

S

S

I

L

I

V

G

G

Q

K

D

H

L

M

S

K

T

Q

F

Y

Y

I

-
x
G

-

I

-

A

-

G

R

T

P

M

Y

F

T

T

A

T

L

L

I

A

K

E

N

E

K

G

I

I

I

N

P

I

I

E

L

M

F

I

N

S

N

Q

T

G

V

A

T

N

G

E

K

I

N

N

V

I

S

S

L

C

V

V

V

I

K

N

K

E

S

S

E

D

L

S

N

I

K

K

A

A

L

L

N

Q

V

C

I

I

H
|
H

G

A

E

K

I

L

F

-

G

-

V

L

S

S

K

E

K

R

I

T

N

N

I

T

A

S

-

N

V

Q

F

F

G

E

H

H

G

A

L

I

K18 (= K5) mutation K->R,A,Q: Reduces kcat.
G25 (≠ S12) mutation to D: Decreases affinity for aspartate and ATP.
K26 (≠ N13) mutation to I: Decreases affinity for aspartate and ATP.
E254 (≠ H216) mutation to A: Reduces kcat.
E279 (= E241) mutation to A: Reduces kcat and affects inhibition by threonine.
H292 (= H254) mutation to A: Reduces kcat.
A406 (≠ G345) mutation to T: Decreases enzyme stability.
R419 (≠ I358) mutation to A: Reduces kcat.
G452 (vs. gap) mutation to D: Disrupts threonine binding.
H497 (= H438) mutation to A: Reduces kcat.

O60163 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 55% coverage: 3:442/803 of query aligns to 17:495/519 of O60163

query
sites
O60163

I

V

L

Q

K

K

F

F

G

G

K

T

S

S

L

V

S

-

N

-

G

G

E

K

G

F

I

P

N

I

K

K

V

I

V

A

S

V

I

D

I

V

T

A

D

K

K

E

V

Y

N

L

Q

S

G

T

E

K

K

R

I

V

A

A

I

L

V

V

V

C

S

S

A

A

R

R

G

S

N

T

-

D

-

T

-

K

-

A

-

E

-

G

A

T

T

T

D

T

E

R

L

L

E

I

E

R

I

A

L

T

A

E

V

A

A

A

S

L

K

R

N

P

A

A

-

V

-

G

-

S

-

V

-

H

D

D

Y

L

K

V

S

R

L

I

E

E

Q

T

-

D

-

H

-

V

-

Q

-

A

F

A

K

R

K

D

Y

F

Q

I

Q

Q

D

D

V

V

Y

G

A

I

N

Q

V

D

D

E

L

L

S

I

E

D

E

A

F

F

A

H

V

A

-

D

-

C

-

V

-

E

L

L

D

E

K

Q

L

Y

F

L

E

N

G

A

V

I

S

R

L

V

I

L

G

S

D

E

Y

V

S

S

S

P

K

R

I

T

K

R

D

D

Q

L

I

V

L

I

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G

I

M

G

G

E

E

L

R

L

L

S

S

A

C

K

R

L

F

L

M

T

A

A

A

I

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L

L

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K

E

D

K

Q

G

G

V

I

N

D

A

S

R

E

F

F

A

I

D

D

-

M

-

S

-

H

-

I

-

D

-

E

S

Q

R

R

T

E

F

W

L

R

K

N

T

L

D

D

S

A

K

S

F

F

G

Y

D

A

A

Y

Q

L

P

A

L

S

E

Q

Q

L

V

A

S

S

K

K

K

V

N

T

V

A

I

V

K

-

Y

-

F

-

K

-

D

-

N

-

D

G

D

N

A

K

V

V

N

P

V

V

T

T

G

G

F

F

I

F

G

G

S

M

N

V

I

P

N

G

V

L

T

L

T

S

T

Q

L

I

G

G

R

R

N

G

G

Y

S

T

N

D

Y

F

T

C

A

A

S

A

L

L

A

A

N

V

Y

G

L

L

D

N

A

A

K

D

E

E

L

L

Q

Q

N

I

Y

W

T

K

H

E

V

V

D

D

G

G

I

I

Y

F

T

T

A

A

N

D

P

P

D

R

L

K

V

V

A

P

D

T

A

A

K

R

K

L

I

L

D

P

H

L

L

I

T

T

F

P

N

E

E

E

A

A

N

A

E

E

L

L

A

T

N

Y

F

Y

G

G

A

S

T

E

I

V

L

I

H

H

A

P

K

F

T

T

I

M

I

S

P

Q

L

V

E

H

K

A

N

R

I

I

P

P

L

I

R

R

I

I

L

K

N

N

T

V

F

G

N

N

H

P

E

R

N

G

E

K

G

G

T

T

L

V

-

I

-

F

-

P

-

D

-

T

-

I

-

S

-

R

-

H

-

G

-
x
S

-

A

-
x
T

-

P

-

H

-

P

-

K

-

I

-

M

-

P

-

D

I

I

T

S

A

A

T

S

S

L

K

A

S

N

G

K

G

G

I

A

K

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T

A

L

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S

T

V

I

L

K

E

D

D

T

L

I

A

M

L

V

V

I

N

N

L

I

E

Q

G

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R

N

G

R

L

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L

I

G

S

K

A

T

H

G

G

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F

D

L

A

A

R

S

I

I

F

F

K

A

V

I

M

L

G

D

D

K

N

Y

N

K

I

L

S

A

V

V

S

D

I

L

I

I

S

T

Q

-

G

-

S

T

S

S

E

E

R

V

G

H

I

V

G

S

L

M

V

A

V

L

A

Y

E

E

S

E

Q

S

A

D

T

D

K

G

A

N

M

M

I

H

E

E

L

A

E

F

K

V

E

E

F

L

E

-

N

-

D

-

F

-

Y

-

S

-

K

R

D

R

V

L

N

G

K

T

I

L

S

D

V

I

T

L

D

H

D

G

V

L

S

A

V

I

I

L

S

S

I

L

I

V

G

G

Q

K

D

H

L

M

-

R

-

N

S

T

T

T

F

G

Y

Y

-

A

-

G

R

R

P

M

Y

F

T

C

A

K

L

L

I

A

K

E

N

A

K

Q

I

I

I

N

P

I

I

E

L

M

F

I

N

S

N

Q

T

G

V

A

T

S

G

E

K

I

N

N

V

I

S

S

L

C

V

V

V

I

K

D

K

E

S

K

E

M

L

A

N

V

K

K

A

A

L

L

N

N

V

V

I

I

H

H

G

K

E

E

I

L

F

L

S326 (vs. gap) modified: Phosphoserine
T328 (vs. gap) modified: Phosphothreonine

P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
27% identity, 49% coverage: 3:394/803 of query aligns to 5:351/405 of P61489

query
sites
P61489

I

V

L

Q

K
|
K

F

Y

G
|
G

K

T

S

S

L

V

S

G

N

D

G

L

E

E

G

R

I

I

N

H

K

K

V

V

V

A

S

Q

I

R

I

I

T

A

D

H

K

Y

V

R

N

E

Q

K

G

G

E

H

K

R

I

L

A

A

I

V

V

V

S
|
S

A
|
A

R

M

G

G

N

H

A

T

T
|
T

D

D

E

E

L

L

E

-

I

-

L

I

A

A

V

L

A

A

S

K

K

R

N

-

A

-

D

-

Y

-

K

-

S

-

L

-

E

-

Q

-

F

-

K

-

Y

-

Q

-

D

-

V

-

Y

-

A

-

N

-

V

V

D

N

L

P

S

R

E

P

F

F

A

R

V

E

L

L

D

D

K

L

L

L

F

-

E

-

G

-

V

-

S

-

L

-

I

-

G

-

D

-

Y

-

S

-

K

-

I

-

K

-

D

-

Q

-

I

-

L

T

S

T

I

T

G

G

E
|
E

L

Q

L

V

S

S

A

V

K

A

L

L

T

S

A

M

I

Q

L

L

V

W

E

A

K

M

G

G

V

I

N

P

A

A

R

K

-

G

F

F

A

V

D

Q

S

H

R

Q

T

I

F

G

L

I

K

T

T

T

D

D

S

G

K

R

F

Y

G

G

D

D

A

A

Q

R

P

I

L

L

E

E

Q

-

V

V

S

N

K

P

K

A

N

R

V

I

I

R

K

E

Y

A

F

L

K

-

D

-

N

D

D

Q

D

G

A

F

V

V

N

A

V

V

V

I

T

A

G
|
G

F

F

I

M

G

G

S

T

N

T

I

P

N

E

N

G

V

E

T

I

T

T

L

L

G

G

R
|
R

N

G

G

G

S

S

N
x
D

Y

T

T

T

A

A

S

V

L

A

L

I

A

A

N

A

Y

A

L

L

D

G

A

A

K

K

E

E

L

C

Q

E

N

I

Y

Y

T

T

H
x
D

V

T

D

E

G

G

I

V

Y

Y

T

T

A

T

N
x
D

P

P

D

H

L

L

V

I

A

P

D

E

A

A

K

R

K

K

I

L

D

S

H

V

L

I

T

G

F

Y

N

D

E

Q

A

M

N

L

E

E

L

M

A

A

N

A

F

L

G

G

A

A

T

R

I

V

L

L

H

H

A

P

K

R

T

A

I

V

I

Y

P

Y

L

A

L

K

E

R

K

Y

N

G

I

V

P

V

L

L

R

H

I

V

L

R

N

S

T

S

F

F

N

S

H

Y

E

-

N

N

E

P

G

G

T

T

L

L

I

V

T

K

A

E

T

V

S

A

K

M

S

E

G

M

G

D

I

K

K

A

T

V

L

T

S

G

V

V

L

A

E

L

D

D

L

L

A

D

L

H

V

A

N

Q

L

I

E

G

G

L

R

I

G

G

L

I

L

P

G

D

K

Q

T

P

G

G

V

I

D

A

A

A

R

K

I

V

F

F

K

Q

V

A

M

L

G

A

D

E

N

R

N

G

I

I

S

A

V

V

S

D

I

M

I

I

S

I

Q

Q

G

G

-

V

-

P

-

G

-

H

-

D

S

P

S

S

E

R

R

Q

G

Q

I

M

G

A

L

F

V

T

V

V

A

K

E

K

S

D

Q

F

A

A

T

Q

K

E

A

A

M

L

I

E

E

A

L

L

E

E

K

P

E

-

F

-

E

-

N

-

D

-

F

V

Y

L

S

A

K

E

D

I

V

G

N

G

K

E

I

A

S

I

V

L

T

R

D

P

D

D

V

I

S

A

V

K

I

V

S

S

I

I

I

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G

G

Q

V

D

G

L

L

S

A

T

S

K7 (= K5) mutation to A: Loss of aspartokinase activity.; mutation to M: Loss of aspartokinase activity.
G9 (= G7) mutation to M: Loss of aspartokinase activity.
G10 (= G8) mutation to A: Significant decrease in the catalytic efficiency.
S41 (= S39) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
A42 (= A40) mutation to S: Loss of aspartokinase activity.
T47 (= T45) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
E74 (= E114) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
G135 (= G177) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
R150 (= R192) mutation to A: Significant decrease in the catalytic efficiency.
D154 (≠ N196) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.; mutation to N: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
D174 (≠ H216) mutation to A: Significant decrease in the catalytic efficiency.
D182 (≠ N224) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.

5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
29% identity, 42% coverage: 3:337/803 of query aligns to 4:288/397 of 5yeiC

query
sites
5yeiC

I

V

L

Q

K

K

F

F

G

G

K

T

S

S

L

V

S

G

N

T

G

V

E

E

G

R

I

I

N

E

K

Q

V

V

V

A

S

E

I

K

I

V

T

K

D

K

K

F

V

R

N

E

Q

A

G

G

E

D

K

D

I

V

A

V

I

V

V

V

S

S

A

A

R

M

G

S

N

G

A

E

T

T

D

N

E

R

L

L

E

-

I

-

L

I

A

G

V

L

A

A

S

N

K

Q

N

-

A

-

D

-

Y

-

K

-

S

-

L

I

L

M

E

E

Q

Q

F

P

K

V

K

P

Y

R

Q

E

Q

L

D

D

V

V

Y

-

A

-

N

-

V

-

D

-

L

-

S

-

E

-

F

-

A

-

V

-

L

-

D

-

K

-

L

-

F

-

E

-

G

-

V

-

S

-

L

-

I

-

G

-

D

-

Y

-

S

-

K

-

I

-

K

-

D

-

Q

-

I

M

L

V

S

S

I

T

G

G

E

E

L

Q

L

V

S

T

A

I

K

A

L

L

T

S

A

M

I

A

L

L

V

I

E

K

K

R

G

G

V

V

N

P

A

A

-

V

R

S

F

Y

A

T

D

G

S

N

R

Q

T

V

F

R

L

I

K

L

T

T

D

D

S

S

K

A

F

H

G

T

D

K

A

A

Q

R

P

I

L

L

E

-

Q

H

V

I

S

D

K

D

K

T

N

H

V

I

I

R

K

A

Y

D

F

L

K

K

D

A

N

G

D

R

D

-

A

-

V

V

N

V

V

V

T

A

G

G

F

F

I

Q

G

G

S

V

N

D

I

G

N

N

N

G

V

N

T

I

T

T

L

L

G

G

R

R

N

G

G

G

S

S

N

D

Y

T

T

T

A

G

S

V

L

A

L

L

A

A

N

A

Y

A

L

L

D

K

A

A

K

D

E

E

L

C

Q

Q

N

I

Y

Y

T

T

H

D

V

V

D

D

G

G

I

V

Y

Y

T

T

A

T

N

D

P

P

D

R

L

V

V

V

A

P

D

Q

A

A

K

R

I

L

D

D

H

K

L

I

T

T

F

F

N

E

E

E

A

M

N

L

E

E

L

M

A

A

N

S

F

L

G

G

A

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I

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Q

A

I

K

R

T

A

I

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I

E

P

F

L

A

L

G

E

K

K

Y

N

N

I

V

P

P

L

L

R

R

I

V

L

L

N

H

T

S

F

F

N

-

H

Q

E

E

N

G

E

P

G

G

T

T

L

L

I

I

T

T

A

I

T

D

S

P

K

I

S

I

G

S

G

G

I

I

K

-

T

-

L

-

S

A

V

F

L

N

E

R

D

D

L

E

A

A

L

K

V

L

N

T

L

I

E

-

G

-

R

R

G

G

L

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L

P

G

D

K
x
T

T
x
P

G

G

V

V

D
x
A

A

F

R

K

I

I

F

L

K

G

V

P

M

I

G

S

D

A

N

A

N

N

I

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E

V

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D

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M

I

I

S

V

Q
|
Q

binding threonine: T265 (≠ K314), P266 (≠ T315), A269 (≠ D318), Q288 (= Q337)

Sites not aligning to the query:

binding lysine: 342, 345, 346, 347, 348, 349, 350
binding threonine: 362, 363

P26512 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see 2 papers)
27% identity, 47% coverage: 3:378/803 of query aligns to 5:349/421 of P26512

query
sites
P26512

I

V

L

Q

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K

F

Y

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G

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S

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A

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Y

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-

E

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-

F

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Y

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Y

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N

-

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-

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-

A

-

V

-

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D

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L

-

F

-

E

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A

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A

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A

A

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A

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A

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F

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A

F

G

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L

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A

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-

V

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P

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G

N

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A

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-

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C

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I

V

V

T

A

G

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F

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G

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N

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N

E

N

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-

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T

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L

G

G

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G

G

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Y

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A

A

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A

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A

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A

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A

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Y

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T

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A

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A

A

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E

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A

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A

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G

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A

L

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Y

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A

L

R

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A

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F

N

N

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P

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L

R

R

I

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L

R

N

S

T

S

F

Y

N

S

H

N

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-

N

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E

P

G

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L

L

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A

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G

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I

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-

S

A

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V

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L

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G

L

V

A

A

L

T

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D

N

K

L

S

E

E

G

A

R

K

-

V

-

T

-

V

-

L

G

G

L

I

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P

G
|
G

V

E

D
x
A

A

A

R

K

I

V

F

F

K

R

V

A

M

L

G

A

D

D

N

A

N

E

I

I

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V

I

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I

M

I

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|
Q

-

N

-

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G
x
S

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D

G

G

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D

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F

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D

A

G

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R

A

A

M

M

-

E

-

I

-

L

-

K

I

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E

Q

L

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E

Q

K

G

E

N

F

W

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L

G277 (= G316) mutation to A: Change in the inhibitory profile upon addition of threonine.
A279 (≠ D318) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
Q298 (= Q337) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
S301 (≠ G338) mutation to F: Absence of inhibition upon addition of threonine and lysine or lysine alone.; mutation to Y: Feedback-resistant and enhanced expression of the asd gene.

Sites not aligning to the query:

360 V→A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
361 T→A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
363 E→A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
364 F→A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.

P41398 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium flavescens (see paper)
27% identity, 47% coverage: 3:378/803 of query aligns to 5:349/421 of P41398

query
sites
P41398

I

V

L

Q

K

K

F

Y

G

G

K

S

S

S

L

L

S

E

N

S

G

A

E

E

G

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I

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R

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A

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D

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A

V

I

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V

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S

A

A

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G

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D

A

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T

T

D

D

E

E

L

L

E

L

E

E

I

L

L

A

A

A

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A

A

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N

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P

N

V

A

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P

Y

A

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L

-

E

-

Q

-

F

-

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-

Y

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-

Y

-

A

-

N

-

V

-

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S

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F

-

A

-

V

-

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F

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G

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G

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Y

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K

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D

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M

I

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L

L

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T

I

A

G

G

E

E

L

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L

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S

A

N

K

A

L

L

L

V

T

A

A

M

I

A

L

I

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E

E

S

K

L

G

G

V

A

N

E

A

A

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-

S

F

F

A

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G

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S

R

Q

T

A

F

G

L

V

K

L

T

T

D

T

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E

K

R

F

H

G

G

D

N

A

A

Q

R

P

I

L

V

E

D

Q

-

V

V

S

T

K

P

K

G

N

R

V

V

I

R

K

E

Y

A

F

L

K

-

D

-

N

D

D

E

D

G

A

K

V

I

N

C

V

I

V

V

T

A

G

G

F

F

I

Q

G

G

S

V

N

N

I

K

N

E

N

T

V

R

-

D

T

V

T

T

L

L

G

G

R

R

N

G

G

G

S

S

N

D

Y

T

T

T

A

A

S

V

L

A

L

L

A

A

N

A

Y

A

L

L

D

N

A

A

K

D

E

V

L

C

Q

E

N

I

Y

Y

T

S

H

D

V

V

D

D

G

G

I

V

Y

Y

T

T

A

A

N

D

P

P

D

R

L

I

V

V

A

P

D

N

A

A

K

Q

K

K

I

L

D

E

H

K

L

L

T

S

F

F

N

E

E

E

A

M

N

L

E

E

L

L

A

A

N

A

F

V

G

G

A

S

T

K

I

I

L

L

H

V

A

L

K

R

T

S

I

V

I

E

P

Y

L

A

L

R

E

A

K

F

N

N

I

V

P

P

L

L

R

R

I

V

L

R

N

S

T

S

F

Y

N

S

H

N

E

-

N

D

E

P

G

G

T

T

L

L

I

I

T

A

A

G

T

S

S

M

K

E

S

D

G

I

G

P

I

V

K

E

T

E

L

-

S

A

V

V

L

L

E

T

D

G

L

V

A

A

L

T

V

D

N

K

L

S

E

E

G

A

R

K

-

V

-

T

-

V

-

L

G

G

L

I

L

S

G

D

K

K

T

P

G

G

V

E

D

A

A

A

R

K

I

V

F

F

K

R

V

A

M

L

G

A

D

D

N

A

N

E

I

I

S

N

V

I

S

D

I

M

I

V

S

L

Q

Q

-

N

-

V

G

S

S

S

S

V

E

E

R

D

G

G

-

T

-

D

I

I

G

T

L

F

V

T

V

C

A

P

E

R

S

A

Q

D

A

G

T

R

K

R

A

A

M

M

-

E

-

I

-

L

-

K

I

L

E

Q

L

V

E

Q

K

G

E

N

F

W

E

T

N

N

D

V

F

L

Y

Y

S

D

K

D

D

Q

V

V

N
x
D

K

K

I

V

S

S

V

L

D345 (≠ N374) mutation to G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.

Query Sequence

>WP_066328676.1 NCBI__GCF_900100165.1:WP_066328676.1
MKILKFGGKSLSNGEGINKVVSIITDKVNQGEKIAIVVSARGNATDELEEILAVASKNAD
YKSLLEQFKKYQQDVYANVDLSEEFAVLDKLFEGVSLIGDYSSKIKDQILSIGELLSAKL
LTAILVEKGVNARFADSRTFLKTDSKFGDAQPLEQVSKKNVIKYFKDNDDAVNVVTGFIG
SNINNVTTTLGRNGSNYTASLLANYLDAKELQNYTHVDGIYTANPDLVADAKKIDHLTFN
EANELANFGATILHAKTIIPLLEKNIPLRILNTFNHENEGTLITATSKSGGIKTLSVLED
LALVNLEGRGLLGKTGVDARIFKVMGDNNISVSIISQGSSERGIGLVVAESQATKAMIEL
EKEFENDFYSKDVNKISVTDDVSVISIIGQDLSTFYRPYTALIKNKIIPILFNNTVTGKN
VSLVVKKSELNKALNVIHGEIFGVSKKINIAVFGHGLVGGTLINQILESAKAIEKRKDIK
LNIFAIANSKNVLLNKDGVSPNWVNEIQTNGFAYTIKDVIAYANENHLENLIAVDNTASA
AFVENYIPLVENGFDLISSNKVANTLSYGFYKELRKVLAENQKNYLYETNVGAGLPLIDT
IKLLHLSGENITKIKGVFSGTLSYLFNNFSAKDAPFSDILKEAIDNGYTEPDPREDLCGN
DVGRKLLILARELDLQNEFEEIAIQNLIPEHLREGSAADFLTKLKEFDPIYTKIKEEQKP
NHVLRYIGELSGDLQNDKGILEVKLVSVPSDTALGGLKGSDSFFEIYTESYGDRPIVIQG
AGAGSAVTARGVFGDILRLSDKG

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory